2D3W

Crystal Structure of Escherichia coli SufC, an ATPase compenent of the SUF iron-sulfur cluster assembly machinery

2D3W の概要

• エントリーDOI: 10.2210/pdb2d3w/pdb
• 分子名称: Probable ATP-dependent transporter sufC (2 entities in total)
• 機能のキーワード: abc-atpase, abc-transporter, iron-sulfur cluster, sufc, biosynthetic protein
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cytoplasm: P77499
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 110453.33

構造登録者

Kitaoka, S.,Wada, K.,Hasegawa, Y.,Minami, Y.,Takahashi, Y.,Fukuyama, K. (登録日: 2005-10-03, 公開日: 2006-01-17, 最終更新日: 2024-03-13)

主引用文献

Kitaoka, S.,Wada, K.,Hasegawa, Y.,Minami, Y.,Fukuyama, K.,Takahashi, Y.
Crystal structure of Escherichia coli SufC, an ABC-type ATPase component of the SUF iron-sulfur cluster assembly machinery
Febs Lett., 580:137-143, 2006

PubMed Abstract: SufC is an ATPase component of the SUF machinery, which is involved in the biosynthesis of Fe-S clusters. To gain insight into the function of this protein, we have determined the crystal structure of Escherichia coli SufC at 2.5A resolution. Despite the similarity of the overall structure with ABC-ATPases (nucleotide-binding domains of ABC transporters), some key differences were observed. Glu171, an invariant residue involved in ATP hydrolysis, is rotated away from the nucleotide-binding pocket to form a SufC-specific salt bridge with Lys152. Due to this salt bridge, D-loop that follows Glu171 is flipped out to the molecular surface, which may sterically inhibit the formation of an active dimer. Thus, the salt bridge may play a critical role in regulating ATPase activity and preventing wasteful ATP hydrolysis. Furthermore, SufC has a unique Q-loop structure on its surface, which may form a binding site for its partner proteins, SufB and/or SufD.

PubMed: 16364320
DOI: 10.1016/j.febslet.2005.11.058

実験手法

X-RAY DIFFRACTION (2.5 Å)